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SERC5_MACFA
ID   SERC5_MACFA             Reviewed;         424 AA.
AC   Q4R6L9; G7P7U7;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=Serine incorporator 5;
GN   Name=SERINC5; ORFNames=EGM_15191, QtsA-17704 {ECO:0000303|Ref.1};
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CE-4;
RX   PubMed=22002653; DOI=10.1038/nbt.1992;
RA   Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N., Li Q.,
RA   Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P., Huang Z.,
RA   Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T., Huang Y.,
RA   Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D., Li B., Liu X.,
RA   Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X., Li Y., Wang W.,
RA   Katze M.G., Su B., Nielsen R., Yang H., Wang J., Wang X., Wang J.;
RT   "Genome sequencing and comparison of two nonhuman primate animal models,
RT   the cynomolgus and Chinese rhesus macaques.";
RL   Nat. Biotechnol. 29:1019-1023(2011).
CC   -!- FUNCTION: Restriction factor required to restrict infectivity of
CC       gammaretroviruses: acts by inhibiting early step of viral infection and
CC       impairing the ability of the viral particle to translocate its content
CC       to the cytoplasm (By similarity). Enhances the incorporation of serine
CC       into phosphatidylserine and sphingolipids. May play a role in providing
CC       serine molecules for the formation of myelin glycosphingolipids in
CC       oligodendrocytes (By similarity). {ECO:0000250|UniProtKB:Q63175,
CC       ECO:0000250|UniProtKB:Q86VE9}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q86VE9};
CC       Multi-pass membrane protein {ECO:0000255}. Note=Localizes to the cell
CC       membrane, where it is efficiently incorporated into budding
CC       gammaretrovirus virions and impairs subsequent virion penetration of
CC       susceptible target cells. {ECO:0000250|UniProtKB:Q86VE9}.
CC   -!- SIMILARITY: Belongs to the TDE1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EHH54368.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB169164; BAE01256.1; -; mRNA.
DR   EMBL; CM001281; EHH54368.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; NP_001271589.1; NM_001284660.1.
DR   AlphaFoldDB; Q4R6L9; -.
DR   SMR; Q4R6L9; -.
DR   STRING; 9541.XP_005557324.1; -.
DR   GeneID; 101925282; -.
DR   CTD; 256987; -.
DR   eggNOG; KOG2592; Eukaryota.
DR   Proteomes; UP000009130; Chromosome 6.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0051607; P:defense response to virus; ISS:UniProtKB.
DR   GO; GO:0009597; P:detection of virus; ISS:UniProtKB.
DR   GO; GO:0045087; P:innate immune response; ISS:UniProtKB.
DR   GO; GO:0042552; P:myelination; IEA:InterPro.
DR   GO; GO:0006658; P:phosphatidylserine metabolic process; IEA:InterPro.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006665; P:sphingolipid metabolic process; IEA:InterPro.
DR   InterPro; IPR029555; Serinc5.
DR   InterPro; IPR005016; TDE1/TMS.
DR   PANTHER; PTHR10383; PTHR10383; 1.
DR   PANTHER; PTHR10383:SF16; PTHR10383:SF16; 1.
DR   Pfam; PF03348; Serinc; 1.
PE   2: Evidence at transcript level;
KW   Antiviral defense; Cell membrane; Glycoprotein; Immunity; Innate immunity;
KW   Lipid biosynthesis; Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW   Phospholipid metabolism; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..424
FT                   /note="Serine incorporator 5"
FT                   /id="PRO_0000330631"
FT   TOPO_DOM        1..6
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        7..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        24..52
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        53..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        74..87
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        88..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        109..119
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        120..140
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        141..161
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        162..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        183..193
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        194..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        215..221
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        222..242
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        243..274
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        275..295
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        296..348
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        349..369
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        370..391
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        392..412
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        413..424
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        76
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        146
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   424 AA;  47420 MW;  A6CF0E1140B3C680 CRC64;
     MYALYFILVV VLCCIMMSTT VAHKMKEHIP FFEDMCKGIK AGDTCEKLVG YSAVYRVCFG
     MACFFFIFCL LTLKINNSKS CRAHIHNGFW FFKLLLLGAM CSGAFFIPDQ DTFLNAWRYV
     GAVGGFLFIG IQLLLLVEFA HKWNKNWTAG TASNKLWYAS LALVTLIMYS IATGGLVLMA
     VFYTQKDGCM ENKILLGVNG GLCVLISLVA ISPCVQNRQP HSGLLQSGVI SCYVTYLTFS
     ALSSKPAEVV LDEHGKNVTI CVPDFGQDLY RDENLVTILG TSLLIGCILY SCLTSTTRSS
     SDALQGRYAA PELEIARCCF CFSPGGEDTE EQQQGKEGPR VIYDEKKGTV YIYSYFHFVF
     FLASLYVMMT VTNWFNYESA NIESFFSGSW SIFWVKMASC WICVLLYLCT LVAPLCCPTR
     EFSV
 
 
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